==== Secondary Structure Definition by the program DSSP, updated CMBI version by ElmK / April 1,2000 ==== DATE=20-JUL-2011 . REFERENCE W. KABSCH AND C.SANDER, BIOPOLYMERS 22 (1983) 2577-2637 . HEADER HYDROLASE/HYDROLASE INHIBITOR 15-SEP-00 1E81 . COMPND 2 MOLECULE: ENDOTHIAPEPSIN; . SOURCE 2 ORGANISM_SCIENTIFIC: ENDOTHIA PARASITICA; . AUTHOR J.A.READ,J.B.COOPER,L.TOLDO,F.RIPPMANN,P.RADDATZ . 330 1 1 1 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) . 13361.0 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) . 240 72.7 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(J) , SAME NUMBER PER 100 RESIDUES . 19 5.8 TOTAL NUMBER OF HYDROGEN BONDS IN PARALLEL BRIDGES, SAME NUMBER PER 100 RESIDUES . 101 30.6 TOTAL NUMBER OF HYDROGEN BONDS IN ANTIPARALLEL BRIDGES, SAME NUMBER PER 100 RESIDUES . 2 0.6 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-5), SAME NUMBER PER 100 RESIDUES . 1 0.3 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-4), SAME NUMBER PER 100 RESIDUES . 3 0.9 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-3), SAME NUMBER PER 100 RESIDUES . 0 0.0 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-2), SAME NUMBER PER 100 RESIDUES . 0 0.0 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-1), SAME NUMBER PER 100 RESIDUES . 0 0.0 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+0), SAME NUMBER PER 100 RESIDUES . 0 0.0 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+1), SAME NUMBER PER 100 RESIDUES . 54 16.4 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES . 36 10.9 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+3), SAME NUMBER PER 100 RESIDUES . 17 5.2 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+4), SAME NUMBER PER 100 RESIDUES . 2 0.6 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+5), SAME NUMBER PER 100 RESIDUES . 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 *** HISTOGRAMS OF *** . 0 0 0 1 2 0 0 1 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 RESIDUES PER ALPHA HELIX . 1 0 3 1 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 PARALLEL BRIDGES PER LADDER . 3 4 3 3 4 1 1 0 0 0 1 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 ANTIPARALLEL BRIDGES PER LADDER . 1 0 1 0 1 0 1 1 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 LADDERS PER SHEET . # RESIDUE AA STRUCTURE BP1 BP2 ACC N-H-->O O-->H-N N-H-->O O-->H-N TCO KAPPA ALPHA PHI PSI X-CA Y-CA Z-CA 1 -2 E S 0 0 57 0, 0.0 152,-2.3 0, 0.0 153,-0.4 0.000 360.0 360.0 360.0 157.4 29.4 8.4 25.0 2 -1 E T - 0 0 60 150,-0.2 2,-0.3 151,-0.1 170,-0.2 -0.932 360.0-155.8-143.0 168.9 28.2 8.0 21.4 3 0 E G E -A 171 0A 3 168,-2.1 168,-3.3 -2,-0.3 2,-0.4 -0.995 4.6-172.6-150.1 144.1 29.3 8.5 17.8 4 1 E S E +A 170 0A 60 93,-1.2 2,-0.4 -2,-0.3 166,-0.2 -0.954 9.7 174.2-142.5 114.9 27.6 9.1 14.5 5 2 E A E -A 169 0A 7 164,-2.5 164,-2.5 -2,-0.4 2,-0.3 -0.986 29.5-124.8-124.2 135.0 29.5 9.1 11.1 6 3 E T E -A 168 0A 79 -2,-0.4 2,-0.4 162,-0.2 162,-0.3 -0.643 23.3-152.0 -77.4 130.9 28.0 9.4 7.6 7 4 E T E -A 167 0A 0 160,-2.2 160,-3.1 -2,-0.3 12,-0.2 -0.903 10.0-162.2-107.8 132.0 28.9 6.5 5.3 8 5 E T E -F 18 0B 63 10,-2.6 10,-2.9 -2,-0.4 153,-0.0 -0.963 21.9-115.1-119.3 134.9 29.1 7.1 1.6 9 6 E P E -F 17 0B 21 0, 0.0 8,-0.3 0, 0.0 3,-0.1 -0.315 19.1-139.0 -62.4 142.4 29.0 4.6 -1.3 10 7 E I S S+ 0 0 33 6,-2.7 2,-0.3 1,-0.1 7,-0.1 0.692 80.4 5.9 -78.2 -18.5 32.3 4.7 -3.3 11 8 E D S > S- 0 0 58 5,-0.4 3,-1.5 0, 0.0 5,-0.1 -0.920 86.6 -88.4-154.0 176.3 30.4 4.4 -6.6 12 9 E S T 3 S+ 0 0 101 -2,-0.3 -2,-0.0 1,-0.3 0, 0.0 0.484 121.4 58.5 -70.7 -2.6 27.0 4.4 -8.2 13 10 E L T 3 S- 0 0 59 3,-0.1 -1,-0.3 267,-0.0 268,-0.0 0.506 105.2-124.7-103.0 -6.2 26.8 0.6 -7.7 14 11 E D < + 0 0 0 -3,-1.5 -2,-0.1 2,-0.1 3,-0.1 0.905 53.3 157.3 63.0 37.5 27.2 0.7 -3.9 15 12 E D - 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0 0 63 -2,-0.2 2,-0.6 -5,-0.1 -3,-0.2 -0.243 31.4-160.8 -57.2 132.8 43.7 14.6 13.2 28 25 E Q E < -G 23 0C 31 -5,-2.1 -5,-1.7 -4,-0.1 2,-0.6 -0.962 17.8-144.1-113.3 105.4 44.6 12.9 10.0 29 26 E T E +G 22 0C 71 -2,-0.6 2,-0.4 -7,-0.2 -7,-0.2 -0.686 23.8 174.6 -82.9 120.7 41.3 12.1 8.2 30 27 E L E -G 21 0C 1 -9,-2.3 -9,-2.3 -2,-0.6 2,-0.9 -0.949 31.9-125.7-120.9 139.2 41.1 8.8 6.3 31 28 E N E -G 20 0C 56 -2,-0.4 92,-2.6 -11,-0.2 93,-0.6 -0.769 37.1-171.5 -87.4 108.1 38.1 7.3 4.5 32 29 E L E -Gi 19 124C 0 -13,-2.7 -13,-3.0 -2,-0.9 2,-0.8 -0.773 26.2-126.7-105.1 151.8 37.8 3.8 5.9 33 30 E D E - i 0 125C 16 91,-2.3 93,-2.0 -2,-0.3 2,-0.5 -0.826 27.2-136.8 -91.6 105.9 35.6 0.8 4.8 34 31 E F E - i 0 126C 0 -2,-0.8 2,-0.6 -17,-0.4 93,-0.2 -0.554 25.8-172.1 -67.7 116.4 33.8 -0.4 7.9 35 32 E D E > - i 0 127C 9 91,-2.3 93,-3.3 -2,-0.5 3,-1.2 -0.893 24.6-179.0-120.1 107.1 34.0 -4.2 7.8 36 33 E T T 3 S+ 0 0 1 -2,-0.6 159,-0.6 1,-0.2 94,-0.2 0.367 85.4 66.6 -81.8 9.7 32.0 -6.3 10.3 37 34 E G T 3 S+ 0 0 13 92,-0.1 2,-0.3 157,-0.1 -1,-0.2 0.435 103.9 41.5-106.0 -4.0 33.5 -9.3 8.6 38 35 E S < - 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0 0 59 61,-1.9 3,-3.2 1,-0.2 4,-0.4 -0.287 34.8-133.3 -51.4 119.6 55.5 0.8 -0.7 50 47 E A G > S+ 0 0 90 1,-0.3 3,-0.7 2,-0.2 -1,-0.2 0.738 105.6 59.6 -48.5 -28.4 55.4 3.9 -2.8 51 48 E S G 3 S+ 0 0 96 1,-0.2 -1,-0.3 3,-0.0 -2,-0.1 0.660 102.3 52.3 -77.8 -14.7 54.6 1.7 -5.8 52 49 E E G < S+ 0 0 46 -3,-3.2 2,-0.5 64,-0.0 -1,-0.2 0.375 90.8 89.1-105.2 6.8 51.5 0.3 -4.2 53 50 E V < + 0 0 41 -3,-0.7 2,-0.2 -4,-0.4 64,-0.1 -0.906 45.7 169.1-107.2 122.0 49.9 3.7 -3.4 54 51 E D S S- 0 0 111 -2,-0.5 -3,-0.0 63,-0.2 -1,-0.0 -0.588 73.5 -39.5-135.0 74.4 47.7 5.3 -6.1 55 52 E G S S+ 0 0 67 1,-0.3 2,-0.2 -2,-0.2 -2,-0.1 0.444 93.9 135.2 93.6 -0.8 45.8 8.3 -4.9 56 53 E Q - 0 0 12 61,-0.1 2,-0.5 1,-0.1 -1,-0.3 -0.503 62.0-110.0 -80.4 149.9 44.9 7.1 -1.5 57 54 E T - 0 0 72 63,-0.2 2,-0.3 -2,-0.2 -13,-0.3 -0.691 38.3-146.6 -78.3 123.0 45.2 9.3 1.6 58 55 E I - 0 0 61 -2,-0.5 2,-0.5 -15,-0.1 -13,-0.3 -0.738 8.1-128.7 -97.5 145.4 48.1 8.0 3.7 59 56 E Y B -o 45 0D 0 -15,-3.2 -13,-2.2 -2,-0.3 -12,-0.3 -0.754 19.5-155.7 -85.7 122.1 48.4 8.1 7.5 60 57 E T > - 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